OXSR1_HUMAN
ID OXSR1_HUMAN Reviewed; 527 AA.
AC O95747; Q3LR53; Q7Z501; Q9UPQ1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Serine/threonine-protein kinase OSR1;
DE EC=2.7.11.1;
DE AltName: Full=Oxidative stress-responsive 1 protein;
GN Name=OXSR1 {ECO:0000312|HGNC:HGNC:8508};
GN Synonyms=KIAA1101 {ECO:0000312|EMBL:BAA83053.2},
GN OSR1 {ECO:0000312|EMBL:BAA75674.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA75674.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ILE-304.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:BAA75674.1};
RX PubMed=10083736; DOI=10.1007/s100380050121;
RA Tamari M., Daigo Y., Nakamura Y.;
RT "Isolation and characterization of a novel serine threonine kinase gene on
RT chromosome 3p22-21.3.";
RL J. Hum. Genet. 44:116-120(1999).
RN [2] {ECO:0000312|EMBL:BAA83053.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAA83053.2};
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAP97192.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-304 AND THR-425.
RG NIEHS SNPs program;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH08726.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH08726.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAP97192.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 172-527.
RA Ding J.B., Yu L., Gong R.M., Mao N.H., Han X.F., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homologous to human
RT DCHT mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, AUTOPHOSPHORYLATION, ACTIVITY REGULATION, INTERACTION WITH PAK1,
RP AND MUTAGENESIS OF LYS-46.
RX PubMed=14707132; DOI=10.1074/jbc.m313562200;
RA Chen W., Yazicioglu M., Cobb M.H.;
RT "Characterization of OSR1, a member of the mammalian Ste20p/germinal center
RT kinase subfamily.";
RL J. Biol. Chem. 279:11129-11136(2004).
RN [7]
RP FUNCTION, INTERACTION WITH RELL1; RELL2 AND RELT, AND MUTAGENESIS OF
RP LYS-46.
RX PubMed=16389068; DOI=10.1016/j.bbrc.2005.12.033;
RA Cusick J.K., Xu L.-G., Bin L.-H., Han K.-J., Shu H.-B.;
RT "Identification of RELT homologues that associate with RELT and are
RT phosphorylated by OSR1.";
RL Biochem. Biophys. Res. Commun. 340:535-543(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-427, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=22361696; DOI=10.1016/j.jprot.2012.01.030;
RA Stadler C., Hjelmare M., Neumann B., Jonasson K., Pepperkok R., Uhlen M.,
RA Lundberg E.;
RT "Systematic validation of antibody binding and protein subcellular
RT localization using siRNA and confocal microscopy.";
RL J. Proteomics 75:2236-2251(2012).
RN [18]
RP FUNCTION, INTERACTION WITH PLSCR1, AND AUTOPHOSPHORYLATION.
RX PubMed=22052202; DOI=10.1007/s11010-011-1127-4;
RA Cusick J.K., Mustian A., Jacobs A.T., Reyland M.E.;
RT "Identification of PLSCR1 as a protein that interacts with RELT family
RT members.";
RL Mol. Cell. Biochem. 362:55-63(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-310; SER-324; SER-325;
RP SER-339 AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP FUNCTION.
RX PubMed=28688764; DOI=10.1016/j.bbrc.2017.07.022;
RA Moua P., Checketts M., Xu L.G., Shu H.B., Reyland M.E., Cusick J.K.;
RT "RELT family members activate p38 and induce apoptosis by a mechanism
RT distinct from TNFR1.";
RL Biochem. Biophys. Res. Commun. 491:25-32(2017).
RN [23]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-304 AND SER-433.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Phosphorylates RELL1, RELL2 and RELT (PubMed:16389068,
CC PubMed:28688764). Phosphorylates PAK1 (PubMed:14707132). Phosphorylates
CC PLSCR1 in the presence of RELT (PubMed:22052202).
CC {ECO:0000269|PubMed:14707132, ECO:0000269|PubMed:16389068,
CC ECO:0000269|PubMed:22052202, ECO:0000269|PubMed:28688764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:14707132};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14707132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:14707132};
CC -!- ACTIVITY REGULATION: By autophosphorylation on threonine.
CC {ECO:0000269|PubMed:14707132}.
CC -!- SUBUNIT: Interacts with PAK1 (PubMed:14707132). Interacts with chloride
CC channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not with
CC SLC12A4 and SLC12A7, possibly establishing sensor/signaling modules
CC that initiate the cellular response to environmental stress (By
CC similarity). Interacts with RELL1, RELL2 and RELT (PubMed:16389068).
CC Interacts with PLSCR1 in the presence of RELT (PubMed:22052202).
CC {ECO:0000250|UniProtKB:Q6P9R2, ECO:0000269|PubMed:14707132,
CC ECO:0000269|PubMed:16389068, ECO:0000269|PubMed:22052202}.
CC -!- INTERACTION:
CC O95747; Q9Y376: CAB39; NbExp=3; IntAct=EBI-620853, EBI-306905;
CC O95747; O95747: OXSR1; NbExp=3; IntAct=EBI-620853, EBI-620853;
CC O95747; Q8NC24: RELL2; NbExp=7; IntAct=EBI-620853, EBI-10269209;
CC O95747; P55011: SLC12A2; NbExp=3; IntAct=EBI-620853, EBI-2801449;
CC O95747; Q9H4A3: WNK1; NbExp=8; IntAct=EBI-620853, EBI-457907;
CC O95747; Q96J92: WNK4; NbExp=12; IntAct=EBI-620853, EBI-766352;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22361696}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissue examined.
CC {ECO:0000269|PubMed:10083736}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:14707132,
CC ECO:0000269|PubMed:22052202}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP97192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA83053.2; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/oxsr1/";
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DR EMBL; AB017642; BAA75674.1; -; mRNA.
DR EMBL; AB029024; BAA83053.2; ALT_FRAME; mRNA.
DR EMBL; DQ201638; ABA27097.1; -; Genomic_DNA.
DR EMBL; BC008726; AAH08726.1; -; mRNA.
DR EMBL; AF087893; AAP97192.1; ALT_INIT; mRNA.
DR CCDS; CCDS2675.1; -.
DR RefSeq; NP_005100.1; NM_005109.2.
DR PDB; 2V3S; X-ray; 1.70 A; A/B=433-527.
DR PDB; 2VWI; X-ray; 2.15 A; A/B/C/D=1-303.
DR PDB; 3DAK; X-ray; 2.25 A; A/B/C/D=6-295.
DR PDB; 7OKW; X-ray; 1.62 A; A/B=423-527.
DR PDBsum; 2V3S; -.
DR PDBsum; 2VWI; -.
DR PDBsum; 3DAK; -.
DR PDBsum; 7OKW; -.
DR AlphaFoldDB; O95747; -.
DR SMR; O95747; -.
DR BioGRID; 115269; 147.
DR CORUM; O95747; -.
DR DIP; DIP-34977N; -.
DR ELM; O95747; -.
DR IntAct; O95747; 35.
DR MINT; O95747; -.
DR STRING; 9606.ENSP00000311713; -.
DR BindingDB; O95747; -.
DR ChEMBL; CHEMBL1163104; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O95747; -.
DR iPTMnet; O95747; -.
DR PhosphoSitePlus; O95747; -.
DR SwissPalm; O95747; -.
DR BioMuta; OXSR1; -.
DR EPD; O95747; -.
DR jPOST; O95747; -.
DR MassIVE; O95747; -.
DR MaxQB; O95747; -.
DR PaxDb; O95747; -.
DR PeptideAtlas; O95747; -.
DR PRIDE; O95747; -.
DR ProteomicsDB; 51019; -.
DR Antibodypedia; 2101; 548 antibodies from 37 providers.
DR DNASU; 9943; -.
DR Ensembl; ENST00000311806.8; ENSP00000311713.3; ENSG00000172939.9.
DR GeneID; 9943; -.
DR KEGG; hsa:9943; -.
DR MANE-Select; ENST00000311806.8; ENSP00000311713.3; NM_005109.3; NP_005100.1.
DR UCSC; uc003chy.4; human.
DR CTD; 9943; -.
DR DisGeNET; 9943; -.
DR GeneCards; OXSR1; -.
DR HGNC; HGNC:8508; OXSR1.
DR HPA; ENSG00000172939; Low tissue specificity.
DR MIM; 604046; gene.
DR neXtProt; NX_O95747; -.
DR OpenTargets; ENSG00000172939; -.
DR PharmGKB; PA134973207; -.
DR VEuPathDB; HostDB:ENSG00000172939; -.
DR eggNOG; KOG0582; Eukaryota.
DR GeneTree; ENSGT00940000162134; -.
DR HOGENOM; CLU_000288_111_1_1; -.
DR InParanoid; O95747; -.
DR OMA; TSNCKQG; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; O95747; -.
DR TreeFam; TF105339; -.
DR PathwayCommons; O95747; -.
DR SignaLink; O95747; -.
DR SIGNOR; O95747; -.
DR BioGRID-ORCS; 9943; 18 hits in 1117 CRISPR screens.
DR ChiTaRS; OXSR1; human.
DR EvolutionaryTrace; O95747; -.
DR GeneWiki; OXSR1; -.
DR GenomeRNAi; 9943; -.
DR Pharos; O95747; Tbio.
DR PRO; PR:O95747; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O95747; protein.
DR Bgee; ENSG00000172939; Expressed in buccal mucosa cell and 207 other tissues.
DR ExpressionAtlas; O95747; baseline and differential.
DR Genevisible; O95747; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0071476; P:cellular hypotonic response; IEA:Ensembl.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:BHF-UCL.
DR GO; GO:0038116; P:chemokine (C-C motif) ligand 21 signaling pathway; ISS:BHF-UCL.
DR GO; GO:0038146; P:chemokine (C-X-C motif) ligand 12 signaling pathway; IMP:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0007231; P:osmosensory signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IMP:ParkinsonsUK-UCL.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR028749; Oxsr1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF1; PTHR48012:SF1; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..527
FT /note="Serine/threonine-protein kinase OSR1"
FT /id="PRO_0000086456"
FT DOMAIN 17..291
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 315..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 23..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1W9,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:14707132"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT VARIANT 304
FT /note="T -> I (in dbSNP:rs6599079)"
FT /evidence="ECO:0000269|PubMed:10083736,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.3"
FT /id="VAR_023232"
FT VARIANT 425
FT /note="S -> T (in dbSNP:rs35295772)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025181"
FT VARIANT 433
FT /note="P -> S (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040969"
FT MUTAGEN 46
FT /note="K->A: Loss of autophosphorylation and kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:14707132,
FT ECO:0000269|PubMed:16389068"
FT MUTAGEN 46
FT /note="K->M: Loss of RELT, RELL1 and RELL2 phosphorylation.
FT Retention of some autophosphorylation activity may be due
FT to complex formation with other endogenous kinases in the
FT assay."
FT /evidence="ECO:0000269|PubMed:14707132,
FT ECO:0000269|PubMed:16389068"
FT CONFLICT 316
FT /note="K -> R (in Ref. 5; AAP97192)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> G (in Ref. 5; AAP97192)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="K -> R (in Ref. 5; AAP97192)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3DAK"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2VWI"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2VWI"
FT TURN 50..54
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:2VWI"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2VWI"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 207..222
FT /evidence="ECO:0007829|PDB:2VWI"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:2VWI"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:3DAK"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3DAK"
FT HELIX 262..271
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:2VWI"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:3DAK"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:7OKW"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:7OKW"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:7OKW"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:7OKW"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:7OKW"
FT HELIX 479..491
FT /evidence="ECO:0007829|PDB:7OKW"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:7OKW"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:7OKW"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:2V3S"
FT STRAND 507..511
FT /evidence="ECO:0007829|PDB:2V3S"
FT TURN 515..518
FT /evidence="ECO:0007829|PDB:7OKW"
FT STRAND 519..526
FT /evidence="ECO:0007829|PDB:7OKW"
SQ SEQUENCE 527 AA; 58022 MW; B46EC934E95A3A1F CRC64;
MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK EKVAIKRINL EKCQTSMDEL
LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIVAK GEHKSGVLDE
STIATILREV LEGLEYLHKN GQIHRDVKAG NILLGEDGSV QIADFGVSAF LATGGDITRN
KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL
QNDPPSLETG VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL
QEKTLQRAPT ISERAKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG KAAISQLRSP
RVKESISNSE LFPTTDPVGT LLQVPEQISA HLPQPAGQIA TQPTQVSLPP TAEPAKTAQA
LSSGSGSQET KIPISLVLRL RNSKKELNDI RFEFTPGRDT AEGVSQELIS AGLVDGRDLV
IVAANLQKIV EEPQSNRSVT FKLASGVEGS DIPDDGKLIG FAQLSIS
